ID A0A0U1PZW4_9BURK Unreviewed; 903 AA.
AC A0A0U1PZW4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=AAV94_07050 {ECO:0000313|EMBL:KKW68063.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68063.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW68063.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW68063.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_01897};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKW68063.1}.
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DR EMBL; LBNQ01000023; KKW68063.1; -; Genomic_DNA.
DR RefSeq; WP_046741767.1; NZ_LBNQ01000023.1.
DR AlphaFoldDB; A0A0U1PZW4; -.
DR STRING; 1610491.AAV94_07050; -.
DR PATRIC; fig|1610491.3.peg.1495; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000050580; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000050580};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..507
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 872..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 572..578
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 903 AA; 99897 MW; 2A91CFBEEB03D620 CRC64;
MTEFAKETLP VSLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLY GMHEQNNDWN
RPFRKSARIV GDVMGKYHPH GDSAIYDTIV RMAQPFSLRH MLVDGQGNFG SVDGDNAAAM
RYTEVRLTKI AHELLADIDK ETVDFGPNYD GSEQEPLVLP ARFPNLLVNG SAGIAVGMAT
NIPPHNLSET VNACLHLLHK PDADIDELME FIPAPDFPTG GIIYGMNGVK EGYRTGRGRV
VMRAKVHFED IDRGQRQAII VDELPYQVNK KTLQERMAEL VHEKKLEGIS HIQDESDKSG
MRLVIELKRG EVAEVVLNNL YKQTQLQDTF GINMVALIDG QPRLCNLKDL LQVFLEHRRE
VVTRRTVFEL RKARERGHVL EGLAVALANI DEFIRIIRES PTPPVAKAEL MARSWDSQIV
KQMLTRARED GSVVNADDYR PETLGKQYGL GRDGLYRLSD VQASEILAMR LSRLTGLEQD
KIVAEYKDVM AQIEDLLDIL AKPERVSTII ADELTAIKTE YGDTKLGARR SQIEYSAQDL
STEDLITPVD MVVTLSHSGY IKSQPLSEYR AQRRGGRGKQ ATATKEDDWI DQLFIANTHD
YILCFSDRGR LYWLKVWEVP SGSRGSRGRP IINMFPLAEG EKITVVLPLT GEARKFPDDQ
YVFMATAKGT VKKTALTEFS NPRKAGIIAV GLDEGDYLIG AALTDGKHDV MLFSDNGKAV
RFDENDVRPM GRNARGVRGM NLEEGQSVIA MLVAEAEGDP STQSVLTATE NGYGKRTAIT
EYTRHGRGTK GMIAIQQSER NGKVVAATLV GPDDEIMLIT DTGVLVRTRV AEIRELGRAT
QGVTLIALDE GAKLIGLQRI VENDANGIDS GAQMGLEADA GGANNGEAAQ SGAADEDSSP
TTD
//
